Plant <scp>NLRs</scp> are getting into higher‐order architectures

Nucleotide-binding leucine-rich repeat (NLR) proteins are central components of the plant immune system that detect pathogen-derived effectors or modifications of host proteins within the cell to activate immune responses. NLRs have co-evolved with pathogens in an ongoing evolutionary arms race, leading to diversification of NLR structures and the establishment of highly interconnected immune networks. Recent studies have shown that NLRs dynamically assemble into higher-order structures, including multimeric complexes, filaments, and biomolecular condensates. These higher-order architectures are essential for NLR activation, intracellular signaling, and interactions with host proteins. Structural and biochemical analyses have revealed both conserved and divergent mechanisms underlying these assemblies. In this review, we summarize recent advances in understanding the formation and functional significance of higher-order NLR assemblies.